Argos P
European Molecular Biology Laboratory, Heidelberg, FRG.
Protein Eng. 1988 Jul;2(2):101-13. doi: 10.1093/protein/2.2.101.
Protein structures were collected from the Brookhaven Database of tertiary architectures that displayed oligomeric association (24 molecules) or whose polypeptide folding revealed domains (34 proteins). The subunit and domain interfaces for these proteins were respectively examined from the following aspects: percentage water-accessible surface area buried by the respective associations, surface compositions and physical characteristics of the residues involved in the subunit and domain contacts, secondary structural state of the interface amino acids, preferred polar and non-polar interactions, spatial distribution of polar and non-polar residues on the interface surface, same residue interactions in the oligomeric contacts, and overall cross-section and shape of the contact surfaces. A general, consistent picture emerged for both the domain and subunit interfaces.
蛋白质结构取自布鲁克海文三级结构数据库，这些结构呈现出寡聚缔合（24个分子），或者其多肽折叠显示出结构域（34种蛋白质）。从以下几个方面分别研究了这些蛋白质的亚基和结构域界面：各自缔合所掩埋的可及水表面积百分比、亚基和结构域接触中涉及的残基的表面组成和物理特性、界面氨基酸的二级结构状态、优先的极性和非极性相互作用、界面表面上极性和非极性残基的空间分布、寡聚接触中的相同残基相互作用，以及接触表面的整体横截面和形状。对于结构域和亚基界面，出现了一个总体一致的情况。
